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Binding mode of new (thio)hydantoin inhibitors of fatty acid amide hydrolase: comparison with two original compounds, OL-92 and JP104

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Michaux, Catherine [UNamur] Muccioli, Giulio [UCL] Lambert, Didier [UCL] Wouters, Johan [UNamur]

Substituted (thio)hydantoins (2-thioxoimidazolidinones and imidazolidinediones) were reported as new potential reversible inhibitors of fatty acid amide hydrolase (FAAH). Their binding mode to FAAH was explored to rationalize their activity and give idea to design highly active inhibitors. Starting from the crystal structure of one of these molecules, docking studies provide us with rational basis for the design of new inhibitors within the thiohydantoin family.

Document type Article de périodique (Journal article) – Article de recherche
Access type Accès libre
Publication date 2006
Language Anglais
Journal information "Bioorganic & Medicinal Chemistry Letters : the tetrahedron journal for research at the interface of chemistry and biology" - Vol. 16, no. 18, p. 4772-4776 (2006)
Peer reviewed yes
Publisher Elsevier Science Ltd ((United Kingdom) Oxford)
issn 0960-894X
e-issn 1464-3405
Publication status Publié
Affiliations UCL - SSS/LDRI - Louvain Drug Research Institute
UCL - (SLuc) Service de prothèse dentaire
UCL - MD/FARM - Ecole de pharmacie
MESH Subject Amidohydrolases ; Binding Sites ; Enzyme Inhibitors ; Imidazolidines ; Models, Molecular ; Molecular Structure ; Thiohydantoins
Links
Bibliographic reference Michaux, Catherine ; Muccioli, Giulio ; Lambert, Didier ; Wouters, Johan. Binding mode of new (thio)hydantoin inhibitors of fatty acid amide hydrolase: comparison with two original compounds, OL-92 and JP104. In: Bioorganic & Medicinal Chemistry Letters : the tetrahedron journal for research at the interface of chemistry and biology, Vol. 16, no. 18, p. 4772-4776 (2006)
Permanent URL http://hdl.handle.net/2078.1/141075